We have isolated a human cDNA clone encoding a novel protein of 22 kDa that is a human counterpart of the rat oncoprotein PTTG. We show that the corresponding gene (hpttg) is overexpressed in Jurkat cells (a human T lymphoma cell line) and in samples from patients with different kinds of hematopoietic malignancies. Analysis of the sequence showed that hPTTG has an amino-terminal basic domain and a carboxyl-terminal acidic domain, and that it is a proline-rich protein with several putative SH3-binding sites. Subcellular fractionation studies show that, although hPTTG is mainly a cytosolic protein, it is partially localized in the nucleus. In addition we demonstrate that the acidic carboxyl-terminal region of hPTTG acts as a transactivation domain when fused to a heterologous DNA binding domain, both in yeast and in mammalian cells.
Pubmed ID: 9811450 RIS Download
Mesh terms: Amino Acid Sequence | Animals | Base Sequence | Blotting, Western | COS Cells | Cloning, Molecular | DNA, Complementary | Gene Expression Regulation, Neoplastic | Hematologic Neoplasms | Humans | Jurkat Cells | Molecular Sequence Data | Neoplasm Proteins | Protein Biosynthesis | Rats | Saccharomyces cerevisiae | Securin | Transcription, Genetic | beta-Galactosidase
Publication data is provided by the National Library of Medicine ® and PubMed ®. Data is retrieved from PubMed ® on a weekly schedule. For terms and conditions see the National Library of Medicine Terms and Conditions.